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Comment
. 2010 Oct 19;107(42):17859-60.
doi: 10.1073/pnas.1012923107. Epub 2010 Oct 11.

Scaffolding to build a rational vaccine design strategy

Dennis R Burton  1
Affiliations
Comment

Scaffolding to build a rational vaccine design strategy

Dennis R Burton. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1.
Fig. 1.
The epitope scaffolding strategy. (A) 2F5 is a broadly neutralizing anti-HIV antibody that recognizes a conserved continuous epitope close to the viral membrane on the glycoprotein gp41 of the surface envelope spike. (B) An epitope peptide adopts an extended kinked structure when bound to 2F5, as shown by crystallography. Grafting of the peptide into different scaffolding proteins selected from computational analyses identifies a number that present the epitope in the extended kinked conformation (C) and bind 2F5 tightly (D). (E) Immunization of small animals with scaffolds yields polyclonal antibody responses that match the specificity of 2F5 closely. (F) mAbs from immunized mice recognize the epitope peptide in the extended kinked conformation. (G) However, scaffold-elicited antibodies do not neutralize HIV, indicating that the scaffold design may need modification to induce antibody features (possibly the long H3 loop with hydrophobic character) to allow close approach of antibodies to the viral membrane.
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References

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